scholarly journals PEMISAHAN ASAM AMINO DARI LIMBAH CAIR PABRIK KELAPA SAWIT DENGAN KROMATOGRAFI PENUKAR ION

2018 ◽  
Vol 6 (2) ◽  
pp. 69
Author(s):  
Indah Rahmi Sari ◽  
Ade Ayu Oksari ◽  
Irma Kresnawaty
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Liquid Waste ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Enzyme Hydrolysis ◽  
Protease Enzyme ◽  
Absorbance Reading ◽  
Amino Acid Levels ◽  
Hydrolysis Of

Separation of Amino acid from Liquid waste of Oil palm Factory with Ion Exchange Chromatography Research on Separation of Amino Acid Liquid Waste mills with Ion Exchange Chromatography was carried out from October to November 2015. The results of  hydrolysis of 6 N HCl results showed  that the highest absorbance reading was obtained at a concentration of eluent of 0,2 and 0,6 M NaCl, while the results of the protease enzyme hydrolysis the highest absorbance reading at NaCl eluent 0,2 and 1 M. There was no significant difference in the results of separation by ion exchange chromatography, showed that the concentration of NaCl eluent is not very influential, so for subsequent analysis used only one concentration of the eluent. Results of linear regression obtained was equal to 0,9946, these results indicate that the series standard amino acid lysine has a value that is linear as it approaches 1. The amino acid levels obtained on the sample results LCPKS hydrolysis with 6 N HCl which was about 0 to 8.82 ppm and samples of the protease enzyme hydrolysis of about 0 to 4.31 ppm. Amino acid levels obtained were still far from the expected.Keywords: Amino Acid, Oil Palm, Liquid Waste, Ion Exchange Chromatography ABSTRAKPenelitian mengenai Pemisahan Asam Amino dari Limbah Cair Pabrik Kelapa Sawit dengan Kromatografi Penukar Ion telah dilaksanakan dari bulan Oktober sampai November 2015. Hasil hidrolisis HCl 6 N menunjukkan bahwa pembacaan absorbansi tertinggi diperoleh pada konsentrasi eluen NaCl 0,2 dan 0,6 M, sedangkan hasil hidrolisis enzim protease pembacaan absorbansi tertinggi pada eluen NaCl 0,2 dan 1 M. Tidak ada perbedaan yang signifikan pada hasil pemisahan dengan kromatografi penukar ion ini, menunjukkan bahwa konsentrasi eluen NaCl tidak terlalu berpengaruh, sehingga untuk analisis selanjutnya digunakan hanya satu konsentrasi eluen. Hasil regresi linear yang diperoleh yaitu sebesar 0,9946, hasil tersebut menunjukkan bahwa deret standar asam amino lisin mempunyai nilai yang linear karena mendekati 1. Kadar asam amino yang diperoleh pada sampel hasil hidrolisis LCPKS dengan HCl 6N yaitu sekitar 0 – 8,82 ppm dan sampel hasil hidrolisis enzim protease sekitar 0 – 4,31 ppm. Kadar asam amino yang diperoleh masih jauh dari yang diharapkan.Kata Kunci: Asam Amino, Minyak Kelapa Sawit, Limbah Cair, Kromatografi Penukar Ion

Quantitative Chromatographic Studies on Urinary Amino Acid Excretion

1968 ◽  
Vol 14 (1) ◽  
pp. 12-21 ◽  
Author(s):  
Richard P Geer ◽  
Richard K Hantman ◽  
Cyrus V Swett
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Acid Excretion ◽  
Amino Acid Nitrogen ◽  
Urinary Amino

Abstract Amino acid excretions of 82 individuals were quantitatively determined by ion-exchange chromatography. The results are expressed as µmoles amino acid per day, divided by milligrams α-amino acid nitrogen per day. This index is independent of age and provides a more useful method of representation than those presently employed in the literature.

Effect of Deproteinating Agents (Picric Acid and Sulfosalicylic Acid) on Analysis for Free Amino Acids in Swine Blood and Tissue

1969 ◽  
Vol 52 (5) ◽  
pp. 981-984 ◽  
Author(s):  
J E Knipfel ◽  
D A Christensen ◽  
B D Owen
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Ion Exchange ◽  
Free Amino ◽  
Biological Fluids ◽  
Picric Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Sulfosalicylic Acid ◽  
Coefficients Of Variation

Abstract Amino acid analyses were performed on samples of blood, liver tissue, loin muscle, and ham muscle by ion exchange chromatography after deproteination of the samples with picric acid or sulfosalicylic acid (SSA). Resolution of threonine and serine from the ion exchange column was poor when SSA was used as the deproteinating agent. Twelve of sixteen amino acids were higher (P < 0.05) in serum deproteinated with picric acid as compared to concentrations determined after SSA deproteination. Amino acid values for ham muscle tended to be higher after deproteination with picric acid; however, with liver and loin muscle samples, the values were somewhat higher after SSA deproteination. In both serum and tissue analyses, coefficients of variation were lower for niGSt amino acids when picric acid was utilized as the deproteinating agent. The latter observation, in particular, suggests that picric acid is preferable to SSA as a deproteinating agent before amino acid analyses of biological fluids. Standardization of methods of deproteination is needed to allow meaningful comparisons of data.

scholarly journals Isolation and a partial amino acid sequence of insulin from the islet tissue of cod (Gadus callarias)

1968 ◽  
Vol 106 (2) ◽  
pp. 531-541 ◽  
Author(s):  
P T Grant ◽  
K. B. M. Reid
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Gel Filtration ◽  
Bovine Insulin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Performic Acid ◽  
Amino Acid Residues ◽  
Islet Tissue ◽  
A Chain

1. Insulin has been isolated by gel filtration and ion-exchange chromatography from extracts of the discrete islet tissue of cod. The final preparation yielded a single band on electrophoresis at two pH values. The biological potency was 11·5 international units/mg. in mouse-convulsion and other assay procedures. 2. Glycine and methionine were shown to be the N-terminal amino acids of the A and B chains respectively. An estimate of the molecular weight together with amino acid analyses indicated that cod insulin, like the bovine hormone, consists of 51 amino acid residues. In contrast, the amino acid composition differs markedly from bovine insulin. 3. Oxidation of insulin with performic acid yielded the A and B peptide chains, which were separated by ion-exchange chromatography. Sequence studies on smaller peptides isolated from enzymic digests or from dilute acetic acid hydrolysates of the two chains have established the sequential order of 14 of the 21 amino acid residues of the A chain and 25 of the 30 amino acid residues of the B chain.

Role of Methionine in the Initiation of the Biosynthesis of Bovine Proinsulin

1973 ◽  
Vol 51 (6) ◽  
pp. 783-788 ◽  
Author(s):  
C. C. Yip ◽  
C. C. Liew
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Defined Medium ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Edman Degradation ◽  
Tissue Slices ◽  
Fetal Bovine ◽  
Bovine Pancreas

Slices of fetal bovine pancreas were used to study the initiation of proinsulin biosynthesis. The pancreatic slices were incubated with radioactive methionine, phenylalanine, or leucine, in a defined medium. The incorporation of amino acid into peptides in the tissue slices was measured for 2–3 h. Two types of radioactive peptides, "free" and "blocked," were identified by ion-exchange chromatography. Most of the radioactive "blocked" peptides labelled with [3H]phenylalanine and [35S]methionine were hydrolyzed by proteases, except for about 20% of those labelled with [35S]methionine, which also showed higher resistance to acid hydrolysis.Microsomes were isolated from the tissue slices after incubation and were extracted with acid alcohol. The radioactive proteins in the extract were reacted with a solid immunosorbant against insulin. Analysis of the immunoadsorbed radioactive peptides by Edman degradation showed the presence of both methionine and phenylalanine as the N-termini. It was concluded that methionine was an initiating amino acid in the biosynthesis of bovine proinsulin.

Chemical and serological properties of a cyanogen bromide peptide of southern bean mosaic virus protein

1980 ◽  
Vol 26 (12) ◽  
pp. 1450-1459 ◽  
Author(s):  
J. H. Tremaine ◽  
W. P. Ronald ◽  
E. M. Kelly
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Mosaic Virus ◽  
Cyanogen Bromide ◽  
Tomato Bushy Stunt Virus ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amino Acid Residues ◽  
Southern Bean Mosaic Virus ◽  
Gel Diffusion

Southern bean mosaic virus (SBMV) protein was cleaved with cyanogen bromide and a highly basic peptide, CB-1, was isolated by ion exclusion and ion-exchange chromatography. Twelve peptides were separated from a tryptic digest of CB-1 by ion-exchange chromatography and the composition of these peptides was similar to that of peptides released from EDTA-swollen virus particles by limited tryptic digestion. The composition and N-termini of the tryptic peptides indicated CB-1 was from the N-terminus of SBMV protein and contained 48 amino acid residues. The CB-1 peptide moved rapidly to the cathode in polyacrylamide gel electrophoresis at pH 3.9 and contained nine arginine residues, three lysine residues, and no acidic amino acid residues. It was shown to interact with purified viral RNA, sodium dextran sulfate, and calf thymus DNA.Antiserum to sodium dodecyl sulfate (SDS)-dissociated virus gave a reaction of partial identity between the CB-1 peptide and the SDS-dissociated virus in SDS gel diffusion tests. The CB-1 peptide did not react with antiserum to SDS-dissociated, trypsin-treated virus. Gel diffusion tests conducted in saline agar gels between trypsin-treated virus and SBMV, with SBMV antiserum, did not show differences in their serological properties. Antiserum to the CB-1 peptide conjugated to tomato bushy stunt virus reacted with SBMV but SBMV antiserum did not react with CB-1 or the CB-1-tomato bushy stunt virus conjugate.

The diguanosine nucleotides: do they exist in aquatic fungi?

1977 ◽  
Vol 55 (8) ◽  
pp. 841-846 ◽  
Author(s):  
A. H. Warner ◽  
D. des S. Thomas ◽  
V. Shridhar ◽  
H. D. McCurdy
Keyword(s):  
Ion Exchange ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Aquatic Fungi ◽  
Enzyme Hydrolysis ◽  
Achlya Ambisexualis ◽  
Cast Doubt ◽  
Blastocladiella Emersonii ◽  
Metabolic Regulators

The aquatic fungi Achlya ambisexualis and Blastocladiella emersonii were grown in the presence of 32Pi and the 32P-labeled acid-soluble nucleotide fractions were analyzed by ion-exchange chromatography on DEAE-cellulose. Selected column fractions containing diguanosine tri- and tetra-phosphates (Gp3G and Gp4G) added as chromatographic markers were analyzed further for 32P by chromatography and (or) enzyme hydrolysis. The results of these experiments clearly indicate that neither Gp4G nor Gp3G is synthesized during vegetative growth of these organisms and cast doubt on the hypothesis that diguanosine nucleotides are important metabolic regulators in fungi.

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